In our Facility, we use mass spectrometry to analyze and characterize biomolecules such as proteins and DNA. We also maintain a small molecule unit that analyzes chemical drug candidates synthesized by various researchers. We provide scientific and technical support in these areas. Furthermore, we successfully promote collaborations to increase our understanding of fundamental biological processes, mostly related but not limited to diabetes, digestive and kidney diseases. [unreadable] [unreadable] We provided analyses to more than 50 principal investigators of our Institute. Many of these analyses are considered to be service and do not result in any publication. [unreadable] [unreadable] Nevertheless, some of the identifications that we perform are considered significant scientific contributions. Next to the support that we provide for other investigators, we have also successfully developed an independent research program. [unreadable] [unreadable] The techniques that we have developed for the determination of the secretory proteome of adipocytes have recently been applied to the determination of the secretory proteome of podocytes and the determinatin of the lipid droplet proteome in rat liver cells. [unreadable] [unreadable] We have concluded a study describing the genetic requirements for growth of E. coli on methyl-alph-D-glucopyranoside and the five alpha-D-glucosyl-D-fructose isomers of sucrose.[unreadable] [unreadable] We also have concluded a study on the cerebrospinal fluid proteome associated with chronic fatigue and related syndromes, which yielded the first predictive biomarkers for these syndromes. Using a logisitic model, we found that detection of >1 of a select set of 5 CFS-related proteins predicted CFS status with 80% concordance. [unreadable] [unreadable] Last but not least, we have expanded on our previously established protein-ligand interaction studies using HIV-1 Gag with assembly factors.[unreadable] Using a similar footprinting method, we also studied the hyperphosphorylation-induced conformational changes of full length native and hyperphosphorylated hRPA (human replication protein A). We found that three residues in the DNA binding domain B (K343, R335 and R382) were significantly shielded by hyperphosphorylation when compared to native hRPA. This led us to conclude that significant conformational changes involving the ssDNA binding cleft are induced after hyperphosphorylation.